Recombinant human UBE2E3 protein (Active) (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

UBE2E3 also known as Ubiquitin-conjugating enzyme E2 E3 is a 24 kDa protein that plays an important role in the ubiquitination process facilitating the transfer of ubiquitin to specific substrate proteins. This enzyme is part of the ubiquitin-proteasome system which regulates protein degradation and turnover within the cell. UBE2E3 is expressed in various tissues with significant levels noted in heart liver and brain tissues suggesting its involvement in multiple cellular processes across different bodily systems.

Biological function summary

The Ubiquitin-conjugating enzyme E2 E3 collaborates with E3 ubiquitin ligases to form an enzyme complex important in tagging defective or unneeded proteins for degradation. This tagging involves the covalent attachment of ubiquitin molecules enabling the proteasome to recognize and subsequently break down these proteins. Such a mechanism is fundamental in maintaining protein homeostasis and regulating cellular functions including cell cycle progression and signal transduction. The interaction with different E3 ligases allows UBE2E3 to target a range of substrates based on cellular context and needs.

Pathways

UBE2E3 plays an important role in the proteasome-mediated degradation pathway and is closely associated with the cell cycle pathway. In these pathways UBE2E3 works alongside proteins such as SCF ubiquitin ligases forming a specific tagging and degradation process that controls the levels of proteins involved in cell proliferation and division. Through these pathways UBE2E3 ensures the timely degradation of cyclins and other regulatory proteins preventing abnormal cell growth and ensuring uninterrupted cell cycle transitions.

Aberrations in UBE2E3 function have links to cancer and neurodegenerative disorders. In cancer altered activity of UBE2E3 can lead to the inappropriate stabilization of oncogenic proteins promoting uncontrolled cell division. Moreover UBE2E3's interaction with specific E3 ligases like Mdm2 highlights its role in modulating p53 tumor suppressor stability which is important in cancer development. In neurodegenerative disorders such as Alzheimer's disease dysregulated ubiquitination processes involving UBE2E3 contribute to protein aggregation and neuronal cell death potentially interacting with proteins like tau implicated in disease progression.